Refined crystal structure of the triphosphate conformation of H‐ras p21 at 1.35 A resolution: implications for the mechanism of GTP hydrolysis.

By E. Pai, U. Krengel, G. Petsko, R. Goody, W. Kabsch, A. Wittinghofer. 1990

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From Principal Component to Direct Coupling Analysis of Coevolution in Proteins: Low-Eigenvalue Modes are Needed for Structure Prediction (2012, unknown): “Results are compared to PDB entry 5p21 [48].”
Evolution-Based Functional Decomposition of Proteins (2015, unknown): “The essential characteristics of these proteins are exempliﬁed by the high-resolution atomic structures of both inactive (GDP-bound, PDB 4Q21 (45)) and active (GTP γ S-bound, PDB 5P21 (46)) states of a canonical member of this family, H-Ras.”
Neutron Crystal Structure of RAS GTPase Puts in Question the Protonation State of the GTP γ-Phosphate* (2015, background): “The crystal form with P3221 symmetry is common among x-ray crystal structures of RAS, used originally to describe the nucleotide-binding site in detail and to formulate hypotheses for the GTP hydrolysis reaction (20).”